Cleaved endocan is the product of cathepsin G specific proteolysis of endocan. The major source of cathepsin G is the polymorphonuclear neutrophils. Nevertheless neutrophils must be activated to express activated cathepsin G on the cell surface and to be released in the bloodstream. Circulating cathepsin G is quickly neutralized by a variety of anti-proteases found in plasma. By contrast, membrane cathepsin G remains active, strongly suspected to be highly responsible of endocan cleavage (PubMed studies).
Under normal conditions, cleaved endocan is undetectable in plasma, but increases markedly in severe septic conditions. The human plasma naturally rich in anti-proteases, even in severe septic patients, is unable to cleave the endocan. It is thought that the endocan cleavage results from close contact between endothelial cells and neutrophils, both activated by the inflammatory process. Its small size (14 kDa) suggests an urinary elimination.
A new clinical concept
Cleaved endocan has been detected in the plasma of some severe septic patients whose level is associated with renal dysfunction.
The presence of cleaved endocan in the blood or urine reflects an active vascular inflammatory event, its disappearance could reflect a favourable outcome and vice versa.
Cleaved endocan identifies a neutrophil-dependent inflammatory mechanism through which the disease can progress.
New clinical applications
Cleaved endocan has been detected in the plasma of some severe septic patients whose level is associated with renal dysfunction.
The presence of cleaved endocan in the blood or urine reflects an active vascular inflammatory event, its disappearance could reflect a favourable outcome and vice versa.
Cleaved endocan identifies a neutrophil-dependent inflammatory mechanism through which the disease can progress
New clinical applications
Cleaved endocan assay is available for research use only (DIYEK C1).